US6972318B1ExpiredUtility

Complex of a chaperone protein with amyloid

Individually held — no corporate assignee on recordPriority: Oct 30, 1998Filed: Oct 29, 1999Granted: Dec 6, 2005
Est. expiryOct 30, 2018(expired)· nominal 20-yr term from priority
C07K 14/4711A61P 25/28G01N 33/6896A61K 38/00G01N 2800/2821G01N 2333/4709
23
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Cited by
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References
2
Claims

Abstract

A chaperone protein Q2 and β-amyloid can form a complex. This complex can be detected in a biological sample, such as, for example, tissues or fluids from a mammal. Q2 levels can also be detected in a biological sample. A method for detecting the Q2 level is a biological sample and comparing that level to a normal Q2 level can be used to detect, screen, diagnose, or otherwise determine a person's susceptibility to Alzheimer's disease such as, for example, the presence or absence of Alzheimer's disease, of symptoms of this disease, of factors leading to or associated with this disease, of likelihood of developing this disease, and the like. In one embodiment, a decline in Q2 level correlates to an increased likelihood for developing Alzheimer's disease. In another embodiment, a decline in Q2 level correlates to an increase in β-amyloid aggregation. The method may further include screening for an apolipoprotein E genetype, which is associated with Alzheimer's disease.

Claims

exact text as granted — not AI-modified
1. An isolated complex comprising human chaperone protein ERp57/GRp58; and human β-amyloid 1–42 or human β-amyloid 1–38. 
     
     
       2. The isolated complex of  claim 1 , wherein the complex is glycosylated.

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